Analysis of the cysteine proteinases of Leishmania mexicana and Trypanosoma cruzi using specific antisera |
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Authors: | Colin D. Robertson Javier Martinez Juan-Jose Cazzulo Graham H. Coombs |
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Affiliation: | Laboratory for Biochemical Parasitology, Department of Zoology, University of Glasgow, Glasgow G12 8QQ, Scotland, UK; Instituto de Investigaciones Bioquimicas, Fundacion Campomar, Av. Patricias Argentinas 435, 1405 - Buenos Aires, Argentina |
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Abstract: | Abstract Antisera raised against papain and cysteine proteinases (CPs) purified from Leishmania mexicana and Trypanosoma cruzi have been used to study the proteins in the two parasites. The antisera against the major CP of T. cruzi (cruzipain) not only cross-reacted with known CPs of L. mexicana but also detected stage-specific molecules that may represent previously unrecognised CPs. The binding of the same abtisera to extracts of different life cycle stages of T. cruzi suggested that the stages possess different isoforms of cruzipain. The lack of cross-reactivity of anti-papain antiserum against cruzipain suggests that the major immunogenic epitopes of these CPs are different, whereas the detection of the major CPs of L. mexicana with both heterologous antisera shows that the parasite's enzymes share epitopes with the other CPs. |
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Keywords: | Trypanosoma cruzi Leishmania mexicana Cysteine proteinase Proteinase |
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